ID A0A1Y2N6D1_PSEAH Unreviewed; 662 AA.
AC A0A1Y2N6D1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain {ECO:0000313|EMBL:OSY42721.1};
GN Name=accA1_1 {ECO:0000313|EMBL:OSY42721.1};
GN ORFNames=BG845_00962 {ECO:0000313|EMBL:OSY42721.1};
OS Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia
OS autotrophica).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=2074 {ECO:0000313|EMBL:OSY42721.1, ECO:0000313|Proteomes:UP000194360};
RN [1] {ECO:0000313|EMBL:OSY42721.1, ECO:0000313|Proteomes:UP000194360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 535 {ECO:0000313|EMBL:OSY42721.1,
RC ECO:0000313|Proteomes:UP000194360};
RA Grumaz C., Vainshtein Y., Kirstahler P., Sohn K.;
RT "Pseudonocardia autotrophica DSM535, a candidate organism with high
RT potential of specific P450 cytochromes.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OSY42721.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MIGB01000004; OSY42721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2N6D1; -.
DR STRING; 2074.BG845_00962; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000194360; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000194360}.
FT DOMAIN 2..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 583..658
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 662 AA; 69572 MW; 944DA9DF59BCD516 CRC64;
MTVHKLLVAN RGEIAERIIR SARALDIATV AVHSDPDADA LFVEAADEAV RLPGAAPSET
YLRADRIIEA ARLTGADAIH PGYGFLSENA EFARACADAG ITFVGPPVEA IEAMGSKIAA
KELMEKAGVP VLPGATIDDA EEIDSAAVSA LADGIGYPLL VKAAFGGGGR GMRIVRSAAD
VLDAVTGARR EAASAFGNGT VFLERFVEDP RHVEVQIFGD THGTVVHLFE RECSIQRRYQ
KIVEEAPSPA VDEALRTRLG DAAVAAGAAI GYTGAGTVEF VMAQTGEFFF LEVNTRLQVE
HPVTEEITGL DLVALQIAVA EGEPLPAEVT GATITGHAIE ARLYAEDPSQ DYLPGSGTVH
RFSVPALPGV RVDTGVRDGS VIGTHYDPML AKVIAHGRTR AEAARKLARA LAEAEIHGPV
TNRDLLVAIL REPEFLAGRT DTGYLTRHEP AVLIGPPAES TLAVHALAAA LADQSGRRDG
ARVQRPVPTG WRNVRSASQH AEYRIGDTDL DVSYRLGRGT LEAGVNGTAL AEPAVLGAGP
ERVDLRVGGV RRAVRVHRVG DTVYVDSVLG ASTLTERPRL PEPGTDAAPG SLLAPMPGTV
VRVAAEAGQQ VEQGTVIVVF EAMKMEHSVR APVAGTVARL SVQVGDTVES GEILAVIEEV
EA
//
